[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retinal pigment epithelium; Voelkel H., Schultz J.E., Kurz U.; Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-301. Miyashita N.; "Bos taurus cathepsin L gene."; Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 114-132 AND 293-311. DOI=10.1016/0014-5793(91)80620-I; PubMed=2044774 [NCBI, ExPASy, EBI, Israel, Japan] Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V.; "The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L."; FEBS Lett. 283:329-331(1991).
[5]	PROTEIN SEQUENCE OF 114-132 AND 293-311. TISSUE=Kidney; PubMed=1515067 [NCBI, ExPASy, EBI, Israel, Japan] Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V.; "Bovine cathepsins S and L: isolation and amino acid sequences."; Biol. Chem. Hoppe-Seyler 373:407-412(1992).

Comments

FUNCTION: Important for the overall degradation of proteins in lysosomes.
CATALYTIC ACTIVITY: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds.
SUBCELLULAR LOCATION: Lysosome.
SIMILARITY: Belongs to the peptidase C1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X91755; CAA62870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102312; AAI02313.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB017648; BAA33398.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S15845; S15845.

NP_776457.1; -.

3D structure databases

HSSP

O60911; 1FH0. [HSSP ENTRY / PDB]

SMR

P25975; 21-334.

ModBase

P25975.

Ontologies

GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Genome annotation databases

Ensembl

ENSBTAG00000017077; Bos taurus. [Contig view]

GeneID

281108; -.

KEGG

bta:281108; -.

Phylogenomic databases

HOVERGEN

P25975; -.

Other

BindingDB

P25975; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 117`	`100`	`Activation peptide.`	`PRO_0000026236`
`CHAIN`	`118 289`	`172`	`Cathepsin L1 heavy chain.`	`PRO_0000026237`
`PROPEP`	`290 291`	`2`		`PRO_0000026238`
`CHAIN`	`292 334`	`43`	`Cathepsin L1 light chain.`	`PRO_0000026239`
`ACT_SITE`	`138 138`		`By similarity.`
`ACT_SITE`	`277 277`		`By similarity.`
`ACT_SITE`	`301 301`		`By similarity.`
`CARBOHYD`	`222 222`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`135 178`		`By similarity.`
`DISULFID`	`169 212`		`By similarity.`
`DISULFID`	`270 323`		`Interchain (between heavy and light chains) (By similarity).`
`CONFLICT`	`72 72`		`G -> A (in Ref. 1; CAA62870).`
`CONFLICT`	`116 116`		`K -> W (in Ref. 4 and 5).`
`CONFLICT`	`272 272`		`S -> C (in Ref. 1; CAA62870).`
`CONFLICT`	`305 305`		`P -> G (in Ref. 4 and 5).`
`CONFLICT`	`310 310`		`N -> G (in Ref. 4 and 5).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 37347 Da [This is the MW of the unprocessed precursor]

CRC64: ECA5D7415DDECFC9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPSFFLTVL CLGVASAAPK LDPNLDAHWH QWKATHRRLY GMNEEEWRRA VWEKNKKIID 

        70         80         90        100        110        120 
LHNQEYSEGK HGFRMAMNAF GDMTNEEFRQ VMNGFQNQKH KKGKLFHEPL LVDVPKSVDW 

       130        140        150        160        170        180 
TKKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGKLVS LSEQNLVDCS RAQGNQGCNG 

       190        200        210        220        230        240 
GLMDNAFQYI KDNGGLDSEE SYPYLATDTN SCNYKPECSA ANDTGFVDIP QREKALMKAV 

       250        260        270        280        290        300 
ATVGPISVAI DAGHTSFQFY KSGIYYDPDC SSKDLDHGVL VVGYGFEGTD SNNNKFWIVK 

       310        320        330 
NSWGPEWGWN GYVKMAKDQN NHCGIATAAS YPTV

P25975 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools